EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
2.4.1.346 | isopropyl-1-thio-beta-D-galactopyranoside | - |
Mycolicibacterium smegmatis |
EC Number | Cloned (Comment) | Organism |
---|---|---|
2.4.1.346 | expression in Escherichia coli BL21 | Mycolicibacterium smegmatis |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.4.1.346 | membrane | - |
Mycolicibacterium smegmatis | 16020 | - |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.4.1.345 | Mycolicibacterium smegmatis | A0QWG6 | - |
- |
2.4.1.345 | Mycolicibacterium smegmatis ATCC 700084 | A0QWG6 | - |
- |
2.4.1.346 | Mycolicibacterium smegmatis | A0R043 | - |
- |
2.4.1.346 | Mycolicibacterium smegmatis ATCC 700084 | A0R043 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.4.1.346 | - |
Mycolicibacterium smegmatis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.1.346 | GDP-alpha-D-mannose + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
Mycolicibacterium smegmatis | GDP + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
? | |
2.4.1.346 | GDP-alpha-D-mannose + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
Mycolicibacterium smegmatis ATCC 700084 | GDP + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
? | |
2.4.1.346 | GDP-Man + phosphatidyl-myo-inositol | assay at pH 7.5, 37°C, reaction stopped with CHCl3/CH3OH | Mycolicibacterium smegmatis | ? | - |
? | |
2.4.1.346 | GDP-Man + phosphatidyl-myo-inositol | assay at pH 7.5, 37°C, reaction stopped with CHCl3/CH3OH | Mycolicibacterium smegmatis ATCC 700084 | ? | - |
? | |
2.4.1.346 | additional information | PimB specifically catalyzes the transfer of a mannopyranosyl residue to the 6-position of the myo-inositol ring of phosphatidylinositol | Mycolicibacterium smegmatis | ? | - |
? | |
2.4.1.346 | additional information | PimB specifically catalyzes the transfer of a mannopyranosyl residue to the 6-position of the myo-inositol ring of phosphatidylinositol | Mycolicibacterium smegmatis ATCC 700084 | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.4.1.346 | mannoslytransferase PimB' | - |
Mycolicibacterium smegmatis |
2.4.1.346 | MSMEG_4253 | - |
Mycolicibacterium smegmatis |
2.4.1.346 | PimB | - |
Mycolicibacterium smegmatis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.4.1.346 | 37 | - |
assay at | Mycolicibacterium smegmatis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.4.1.346 | 7.5 | - |
assay at | Mycolicibacterium smegmatis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.4.1.345 | physiological function | both mannosyltransferases PimA and PimB' (MSMEG_4253) recognize phosphatidyl-myo-inositol as a lipid acceptor. PimA specifically catalyzes the transfer of a mannopyranosyl residue to the 2-position of the myo-inositol ring of phosphatidylinositol, whereas PimB' exclusively transfers to the 6-position. PimB' can catalyze the transfer of a mannopyranosyl residue onto the phosphatidylinositol-monomannoside (PIM1) product of PimA, while PimA is unable in vitro to transfer mannopyranosyl onto the PIM1 product of PimB' | Mycolicibacterium smegmatis |
2.4.1.346 | physiological function | both mannosyltransferases PimA and PimB' (MSMEG_4253) recognize phosphatidyl-myo-inositol as a lipid acceptor. PimA specifically catalyzes the transfer of a mannopyranosyl residue to the 2-position of the myo-inositol ring of phosphatidylinositol, whereas PimB' exclusively transfers to the 6-position. PimB' can catalyze the transfer of a mannopyranosyl residue onto the phosphatidylinositol-monomannoside (PIM1) product of PimA, while PimA is unable in vitro to transfer mannopyranosyl onto the PIM1 product of PimB' | Mycolicibacterium smegmatis |